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Protein Page:
H2A.1 (human)
rdtyret
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
H2A.1 Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. Belongs to the histone H2A family. Note: This description may include information from UniProtKB.
Protein type: DNA-binding
Chromosomal Location of Human Ortholog: 6p22.1
Cellular Component: nuclear chromatin; nucleosome; nucleus
Molecular Function: DNA binding; enzyme binding; protein binding; protein heterodimerization activity
Biological Process: chromatin silencing
Reference #:  P0C0S8 (UniProtKB)
Alt. Names/Synonyms: FLJ92027; H2A histone family, member C; H2A.1; H2A/c; H2A1; H2AFC; H2AFD; H2AFI; H2AFN; H2AFP; HIST1H2AG; HIST1H2AI; HIST1H2AK; HIST1H2AL; HIST1H2AM; histone 1, H2ai; histone cluster 1, H2ai; Histone H2A type 1; Histone H2A/p
Gene Symbols: HIST1H2AI
Molecular weight: 13,960 Da
Basal Isoelectric point: 10.9  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

H2A.1

Protein Structure Not Found.


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Sites Implicated In
transcription, induced: T120‑p
transcription, inhibited: S1‑p
activity, inhibited: S1‑p
intracellular localization: T120‑p
molecular association, regulation: T120‑p

Modification Sites and Domains  
Click here to view other types of protein modifications

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
2 2 S1‑p _______sGRGkQGG
9 134 K5‑ac ___sGRGkQGGkARA
2 133 K9‑ac GRGkQGGkARAkAKT
1 2 K13‑ac QGGkARAkAKTRSSR
1 0 R29‑m2 GLQFPVGrVHRLLRk
0 14 K36‑ub rVHRLLRkGNYAERV
1 0 R88 RHLQLAIRNDEELNk
0 9 K95‑ac RNDEELNkLLGkVtI
0 121 K95‑ub RNDEELNkLLGkVtI
0 2 K99‑ac ELNkLLGkVtIAQGG
0 70 K99‑ub ELNkLLGkVtIAQGG
0 10 T101‑p NkLLGkVtIAQGGVL
0 39 K118‑ac IQAVLLPkktESHHk
0 1 K118 IQAVLLPKktESHHk
0 1 K118 IQAVLLPKktESHHk
14 164 K118‑ub IQAVLLPkktESHHk
1 16 K119‑ac QAVLLPkktESHHkA
11 150 K119‑ub QAVLLPkktESHHkA
9 7 T120‑p AVLLPkktESHHkAk
1 132 K125‑ub kktESHHkAkGk___
0 3 K127‑ub tESHHkAkGk_____
0 2 K129‑ub SHHkAkGk_______
2576 : Acetyl-Histone H2A (Lys5) Antibody
  mouse

 
S1‑p _______sGRGkQGG
K5‑ac ___sGRGkQGGkARA
K9‑ac GRGkQGGkARAkAKT
K13‑ac QGGkARAkAKTRSSR
R29 GLQFPVGRVHRLLRk
K36‑ub RVHRLLRkGNYSERV
R88‑m1 RHLQLAIrNDEELNk
K95‑ac rNDEELNkLLGRVtI
K95‑ub rNDEELNkLLGRVtI
R99 ELNkLLGRVtIAQGG
R99 ELNkLLGRVtIAQGG
T101‑p NkLLGRVtIAQGGVL
K118‑ac IQAVLLPkktESHHk
K118‑m1 IQAVLLPkktESHHk
K118‑m2 IQAVLLPkktESHHk
K118‑ub IQAVLLPkktESHHk
K119‑ac QAVLLPkktESHHkA
K119‑ub QAVLLPkktESHHkA
T120‑p AVLLPkktESHHkAK
K125‑ub kktESHHkAKGK___
K127 tESHHkAKGK_____
K129 SHHkAKGK_______
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